Multiple forms of protein kinase CK2 present in leukemic cells: In vitro study of its origin by proteolysis

Roig, Joan; Krehan, Andreas; Colomer, Dolors; Pyerin, Walter; Itarte, Emilio; Plana, Maria

doi:10.1007/978-1-4419-8624-5_28

Cited by 7 publications

(6 citation statements)

References 31 publications

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“…ARC is able to bind to caspase-8 only when it is localized to mitochondria [19]. Calpain I degrades protein kinase CK2 in in vitro leukemic cells [23]. Elevated calpain I expression leads to loss of active protein kinase CK2, which may count for elevation of caspase-8 in AF canine models.…”

Section: Discussionmentioning

confidence: 99%

Anti-apoptotic Effects of a Calpain Inhibitor on Cardiomyocytes in a Canine Rapid Atrial Fibrillation Model

Gong

Sheng

et al. 2009

Cardiovasc Drugs Ther

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Section: Discussionmentioning

confidence: 99%

Anti-apoptotic Effects of a Calpain Inhibitor on Cardiomyocytes in a Canine Rapid Atrial Fibrillation Model

Gong

Sheng

et al. 2009

Cardiovasc Drugs Ther

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“…In vitro, calpain is able to degrade CK2 subunits and could be responsible for regulating the level of CK2 subunits within the cell. 68 Neuron-specific calcium-binding protein hippocalcin and Sorcin, both belonging to the EF-hand family, can associate with the plasma membrane in a Ca 2+ -dependent manner, 69 and in particular, sorcin seems to play a role in multidrug resistance of cancer cells, 70,71 a behavior recently shown to rely, at least partially, on an abnormally high CK2 level. 72 Various Proteins and Enzymes.…”

Section: Discussionmentioning

confidence: 99%

Mass Spectrometry Analysis of a Protein Kinase CK2β Subunit Interactome Isolated from Mouse Brain by Affinity Chromatography

et al. 2008

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CK2, an acronym derived from the misnomer "casein kinase 2", denotes a ubiquitous and extremely pleiotropic Ser/Thr protein kinase, the holoenzyme of which is composed of two catalytic (alpha and/or alpha') and two noncatalytic beta subunits acting as a docking platform and the multifarious functions of which are still incompletely understood. By combining affinity chromatography and mass spectrometry, we have identified 144 mouse brain proteins that associate with immobilized CK2beta. A large proportion (60%) of the identified proteins had been previously reported to be functionally related to CK2, and a similar proportion have been classified as phosphoproteins with approximately half of these having the features of CK2 targets. A large number of the identified proteins ( approximately 40%) either are nuclear or shuttle between the nucleus and cytoplasm, and the biggest functional classes of CK2beta interactors are committed to protein synthesis and degradation (32 proteins) and RNA/DNA interaction (20 proteins). Also well represented are the categories of cytoskeletal/structural proteins (19), trafficking proteins (17), and signaling proteins (14). The identified proteins are examined in relation to their functions and potential as targets and/or regulators of CK2, disclosing in some cases unanticipated links between this kinase and a variety of biochemical events.

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“…CK2 expression and altered protein turnover in myeloid leukemia cells were described in early reports. 49,50 These pioneering studies showed that CK2 was overexpressed in proliferating leukemic blasts of acute myeloid leukemia (AML) as well as CML in blast crisis. 49 Years later, another study showed that CK2a could be a substrate of BCR-ABL and ABL protein tyrosin kinases.…”

Section: Ck2 In Myeloid Tumorsmentioning

confidence: 99%

Protein kinase CK2 in hematologic malignancies: reliance on a pivotal cell survival regulator by oncogenic signaling pathways

et al. 2012

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CK2 is a multitask kinase whose role is essential for a countless number of cellular processes, many of which are critical for blood cell development. A prevailing task for this kinase rests on counteracting programmed cell death triggered by multiple stimuli. CK2 is overexpressed in many solid tumors and in vivo mouse models have proven its tumorigenic potential. Recent data have suggested that CK2 may also have a significant role in the pathogenesis of hematopoietic tumors, such as multiple myeloma, chronic lymphocytic leukemia, acute myelogenous leukemia, acute lymphoblastic leukemia and chronic myeloproliferative neoplasms. CK2 regulates hematopoiesis-associated signaling pathways and seems to reinforce biochemical cascades indispensable for tumor growth, proliferation and resistance to conventional and novel cytotoxic agents. Although its activity is multifold, recent evidence supports the rationale of CK2 inhibition as a therapeutic strategy in solid and hematological tumors and phase-I clinical trials are in progress to test the efficacy of this innovative therapeutic approach. In this review, we will summarize the data supporting CK2 as an oncogenic kinase in blood tumors and we will describe some critical signaling pathways, whose regulation by this protein kinase may be implicated in tumorigenesis. Leukemia (2012Leukemia ( ) 26, 1174Leukemia ( --1179 doi:10.1038/leu.2011; published online 13 January 2012Keywords: hematopoiesis; blood tumors; protein kinase CK2; kinase inhibitors INTRODUCTION Protein kinase CK2 is a highly conserved pleiotropic acidophilic serine-threonine kinase whose essential role in several cellular processes has been increasingly appreciated over the last decade. 1 Structurally, CK2 is a tetrameric enzyme, composed by the assembly of two catalytic (a and/or a') and two regulatory b subunits. The catalytic and regulatory subunits may also be present in the cell as unassembled molecules and it seems that this state is associated with distinct and specific functions. The two catalytic subunits a and a' share 90% sequence homology in their N-terminal region. The regulatory subunit b instead does not have any similarity to the other two subunits. 2 CK2 recognizes motifs characterized by a S/T N-terminal to acidic amino acids, its minimum consensus being S/T-X-X-Ac, where X is any amino acid and Ac is a residue with a carboxylic or phosphorylated side chain (E, D, pS, pY).The spectrum of actions of this kinase is impressive as it can phosphorylate hundreds of substrate proteins, which are involved in disparate cellular processes, such as regulation of cell structure, division, proliferation, programmed death, DNA damage repair, protein translation, gene transcription, organelle function and so forth. 3 It has been estimated that a substantial proportion of the human phosphoproteome (up to 20%) is generated by CK2 alone. For this reason, CK2 has long been viewed as a 'non-targetable' kinase for therapeutic purposes.The essential role of CK2 for cell and organism life is underscored by th...

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Multiple forms of protein kinase CK2 present in leukemic cells: In vitro study of its origin by proteolysis

Cited by 7 publications

References 31 publications

Anti-apoptotic Effects of a Calpain Inhibitor on Cardiomyocytes in a Canine Rapid Atrial Fibrillation Model

Anti-apoptotic Effects of a Calpain Inhibitor on Cardiomyocytes in a Canine Rapid Atrial Fibrillation Model

Mass Spectrometry Analysis of a Protein Kinase CK2β Subunit Interactome Isolated from Mouse Brain by Affinity Chromatography

Protein kinase CK2 in hematologic malignancies: reliance on a pivotal cell survival regulator by oncogenic signaling pathways

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